• 제목/요약/키워드: Helices

검색결과 135건 처리시간 0.04초

CHARACTERIZATIONS OF SPACE CURVES WITH 1-TYPE DARBOUX INSTANTANEOUS ROTATION VECTOR

  • Arslan, Kadri;Kocayigit, Huseyin;Onder, Mehmet
    • 대한수학회논문집
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    • 제31권2호
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    • pp.379-388
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    • 2016
  • In this study, by using Laplace and normal Laplace operators, we give some characterizations for the Darboux instantaneous rotation vector field of the curves in the Euclidean 3-space $E^3$. Further, we give necessary and sufficient conditions for unit speed space curves to have 1-type Darboux vectors. Moreover, we obtain some characterizations of helices according to Darboux vector.

A New Type of Helix Constructed by Plane Curves

  • Choi, Jin Ho
    • Kyungpook Mathematical Journal
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    • 제56권3호
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    • pp.939-949
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    • 2016
  • In this paper, we give an algorithm to construct a space curve in Euclidean 3-space ${\mathbb{E}}^3$ from a plane curve which is called PDP-helix of order d. The notion of the PDP-helices is a generalization of a general helix and a slant helix in ${\mathbb{E}}^3$. It is naturally shown that the PDP-helix of order 1 and order 2 are the same as the general helix and the slant helix, respectively. We give a characterization of the PDP-helix of order d. Moreover, we study some geometric properties of that of order 3.

Leucine Zipper as a Fine Tuner for the DNA Binding; Revisited with Molecular Dynamics Simulation of the Fos-Jun bZIP Complex

  • 최용훈;양철학;김현원;정선호
    • Bulletin of the Korean Chemical Society
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    • 제20권11호
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    • pp.1319-1322
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    • 1999
  • Leucine zipper dynamically tunes the degree of bifurcation of the DNA binding segments in the basic region of the Fos-Jun bZIP complex. Molecular dynamics simulation indicated that site-specific mutagenesis of conserved leucine residues inside the leucine zipper domain caused the change of dynamic behavior of the basic region, and efficient DNA binding occurs only within a certain range of distance between the two DNA binding segments in the basic region. Distribution of α-helices in the hinge region is also suggested to influence the bifurcation of the DNA binding segments.

Engineering a Non-Inhibitory Serpin, Ovalbumin

  • Jeoung, Yeon-Hee;Yu, Myeong-Hee
    • 한국생물물리학회:학술대회논문집
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    • 한국생물물리학회 1997년도 학술발표회
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    • pp.38-38
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    • 1997
  • Serpins (serine protease inhibitor) are single polypeptide proteins of around 400 amino acids, and have a conserved secondary structure consisted of three ${\beta}$-sheets and nine ${\alpha}$-helices. Native conformation of inhibitory serpins is a metastable and requires conformational changes to inhibit target protease.(omitted)

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Identification of new ligands for RNA pseudoknot by structure-based screening of chemical database

  • Park, So-Jung;Jeong, Seung-Hyun;Kim, Yang-Gyun;Park, Hyun-Ju
    • 대한약학회:학술대회논문집
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    • 대한약학회 2003년도 Proceedings of the Convention of the Pharmaceutical Society of Korea Vol.1
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    • pp.254.2-254.2
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    • 2003
  • For many viruses, -1 ribosomal frameshifting regulate protein synthesis using an RNA pseudoknot. The integrity of pseudoknot stability and structure is the important feature for efficient frameshifting. Thus, small molecules interacting with viral RNA pseudoknots would be potential antiviral agents targeting\ulcorner frameshifting system in viruses. X-ray structure of RNA pseudoknot complexed with biotin has been reported, in which biotin is bound at the interface between the pseudoknot's stacked helices. (omitted)

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Relationship between Molecular Structure Characteristics of Feed Proteins and Protein In vitro Digestibility and Solubility

  • Bai, Mingmei;Qin, Guixin;Sun, Zewei;Long, Guohui
    • Asian-Australasian Journal of Animal Sciences
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    • 제29권8호
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    • pp.1159-1165
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    • 2016
  • The nutritional value of feed proteins and their utilization by livestock are related not only to the chemical composition but also to the structure of feed proteins, but few studies thus far have investigated the relationship between the structure of feed proteins and their solubility as well as digestibility in monogastric animals. To address this question we analyzed soybean meal, fish meal, corn distiller's dried grains with solubles, corn gluten meal, and feather meal by Fourier transform infrared (FTIR) spectroscopy to determine the protein molecular spectral band characteristics for amides I and II as well as ${\alpha}$-helices and ${\beta}$-sheets and their ratios. Protein solubility and in vitro digestibility were measured with the Kjeldahl method using 0.2% KOH solution and the pepsin-pancreatin two-step enzymatic method, respectively. We found that all measured spectral band intensities (height and area) of feed proteins were correlated with their the in vitro digestibility and solubility ($p{\leq}0.003$); moreover, the relatively quantitative amounts of ${\alpha}$-helices, random coils, and ${\alpha}$-helix to ${\beta}$-sheet ratio in protein secondary structures were positively correlated with protein in vitro digestibility and solubility ($p{\leq}0.004$). On the other hand, the percentage of ${\beta}$-sheet structures was negatively correlated with protein in vitro digestibility (p<0.001) and solubility (p = 0.002). These results demonstrate that the molecular structure characteristics of feed proteins are closely related to their in vitro digestibility at 28 h and solubility. Furthermore, the ${\alpha}$-helix-to-${\beta}$-sheet ratio can be used to predict the nutritional value of feed proteins.

Redesign of an Interhelical Loop of the Bacillus thuringiensis Cry4B delta-endotoxin for Proteolytic Cleavage

  • Krittanai, Chartchai;Lungchukiet, Panida;Ruangwetdee, Sarinthip;Tuntitippawan, Tipparut;Panyim, Sakol;Katzenmeier, Gerd;Angsuthanasombat, Chanan
    • BMB Reports
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    • 제34권2호
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    • pp.150-155
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    • 2001
  • The mosquito-larvicidal Cry4B protein from Bacillus thuringiensis subsp. israelensds was expressed in Escherichia coli. Upon activation by trypsin, the 130-kDa protoxin was processed into the 65-kDa active toxin containing two polypeptide fragments of ca. 47 and ca. 20 kDa. These two polypeptides are products of internal cleavages on the exposed loop connecting helices 5 and 6 in the seven-helical bundle domain. PCR-based mutagenesis was employed to introduce an additional cleavage site into the loop connecting helices 3 and 4. A series of amino acid changes were introduced into the targeted loop, resulting in seven mutant protoxins. Upon digestion with trypsin, a group of mutants with arginine introduced into the loop (EPRNQ, EPNRNQ, EPRNP, ESRNP and SSRNP) produced polypeptide products similar to those of the wild type (EPNNQ). When the loop, SSRNP, was expanded by an insertion of either asparagine (NSSRNP) or valine (VSSRNP), an additional cleavage was detected with proteolytic products of 47,12 and 6 kDa. This cleavage was confirmed to be at the introduced arginine residue by N-terminal sequencing. The mosquito larvicidal assay against Aedes aegypti demonstrated a relatively unchanged toxicity for the mutants without cleavage and reduced toxicity for those with an additional cleavage.

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BERTRAND CURVES IN NON-FLAT 3-DIMENSIONAL (RIEMANNIAN OR LORENTZIAN) SPACE FORMS

  • Lucas, Pascual;Ortega-Yagues, Jose Antonio
    • 대한수학회보
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    • 제50권4호
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    • pp.1109-1126
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    • 2013
  • Let $\mathbb{M}^3_q(c)$ denote the 3-dimensional space form of index $q=0,1$, and constant curvature $c{\neq}0$. A curve ${\alpha}$ immersed in $\mathbb{M}^3_q(c)$ is said to be a Bertrand curve if there exists another curve ${\beta}$ and a one-to-one correspondence between ${\alpha}$ and ${\beta}$ such that both curves have common principal normal geodesics at corresponding points. We obtain characterizations for both the cases of non-null curves and null curves. For non-null curves our theorem formally agrees with the classical one: non-null Bertrand curves in $\mathbb{M}^3_q(c)$ correspond with curves for which there exist two constants ${\lambda}{\neq}0$ and ${\mu}$ such that ${\lambda}{\kappa}+{\mu}{\tau}=1$, where ${\kappa}$ and ${\tau}$ stand for the curvature and torsion of the curve. As a consequence, non-null helices in $\mathbb{M}^3_q(c)$ are the only twisted curves in $\mathbb{M}^3_q(c)$ having infinite non-null Bertrand conjugate curves. In the case of null curves in the 3-dimensional Lorentzian space forms, we show that a null curve is a Bertrand curve if and only if it has non-zero constant second Frenet curvature. In the particular case where null curves are parametrized by the pseudo-arc length parameter, null helices are the only null Bertrand curves.

Structural and Functional Characterization of CRAMP-18 Derived from a Cathelicidin-Related Antimicrobial Peptide CRAMP

  • Park, Kyong-Soo;Shin, Song-Yub;Hahm, Kyung-Soo;Kim, Yang-Mee
    • Bulletin of the Korean Chemical Society
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    • 제24권10호
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    • pp.1478-1484
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    • 2003
  • CRAMP was identified from a cDNA clone derived from a mouse femoral marrow cells as a member of cathelicidin-derived antimicrobial peptide. Tertiary structure of CRAMP in TFE/$H_2O$ (1 : 1, v/v) solution has been determined by NMR spectroscopy previously and consists of two amphipathic $\alpha-helices$ from Leu4 to Lys10 and from Gly16 to Leu33. These two helices are connected by a flexible region from Gly11 to Gly16. Analysis of series of fragments composed of various portion of CRAMP revealed that an 18-residue fragment with the sequence from Gly16 to Leu33 (CRAMP-18) was found to retain antibacterial activity without cytotoxicity. The effects of two Phe residues at positions 14 and 15 of CRAMP-18 on structure, antibacterial activity, and interaction with lipid membranes were investigated by $Phe^{14,15}$ ${\rightarrow}$ Ala substitution (CRAMP-18-A) in the present study. Substitution of Phe with Ala in CRAMP-18 caused a significant reduction on antibacterial and membrane-disrupting activities. Tertiary structures of CRAMP-18 in 50% TFE/$H_2O$ (1 : 1, v : v) solution shows amphipathic ${\alpha}$-helix, from $Glu^2{\;}to{\;}Leu^{18}$, while CRAMP-18-A has relatively short amphipathic ${\alpha}$-helix from $Leu^4{\;}to{\;}Ala^{15}$. These results suggest that the hydrophobic property of $Phe^{14}{\;}and{\;}Phe^15$ in CRAMP-18 is essential for its antibacterial activity, ${\alpha}$-helical structure, and interactions with phospholipid membranes.

사슬이합체의 헬릭스-코일 구조에 미치는 온도와 변성시약의 영향 (The Effects of Temperature and Denaturant on the Helix-Coil Transition of Chain-Dimer)

  • 김영구;박형석
    • 대한화학회지
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    • 제40권6호
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    • pp.394-400
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    • 1996
  • 결합성 사슬이합체를 형성할 수 있는 올리고펩티드-$(HPPHPPP)_n$-(H: 소수성 아미노산, P: 친수성 아미노산)는 온도, 수소이온 농도, 이온세기, 변성시약 등에 의해 구조적인 변화가 가능하다. 본 연구에서는 변성시약과 온도에 의한 올리고펩티드의 전이 현상을 이론적으로 고찰하였다. 사슬이합체로는 올리고펩티드20R, 변성시약으로는 구아니듐-염산을 사용하였다(20R에는 사슬 내의 정전기적 반발력이 10개가 존재하고, 사슬사이의 정전기적 반발력이 10개가 존재한다). 변성 시약에 의한 올리고펩티드의 나선에서 코일로의 전이는 급격한 것으로 보아, 변성이 일어나는 전이상태에서 올리고펩티드들은 완전한 나선구조와 무질서한 코일구조로만 되어있다. 반면에 온도에 의한 전이는 변성시약에 의한 전이보다 완만하게 일어난다. 낮은 온도에서 긴 나선 구조를 가지는 올리고펩티드가 짧은 나선 구조를 가지는 것보다 다량으로 존재한다. 온도가 증가할수록 부분적으로 변성된 분자들의 몰분율이 증가하여, 전이가 일어나는 온도에서 부분적으로 변성된 올리고펩티드가 널리 분포되어 있다.

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